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Database: UniProt
Entry: V8NJ21_OPHHA
LinkDB: V8NJ21_OPHHA
Original site: V8NJ21_OPHHA 
ID   V8NJ21_OPHHA            Unreviewed;      1416 AA.
AC   V8NJ21;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Collagen alpha-3(IV) chain {ECO:0000313|EMBL:ETE61522.1};
DE   Flags: Fragment;
GN   Name=COL4A3 {ECO:0000313|EMBL:ETE61522.1};
GN   ORFNames=L345_12727 {ECO:0000313|EMBL:ETE61522.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE61522.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE61522.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE61522.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC   -!- FUNCTION: Type IV collagen is the major structural component of
CC       glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork
CC       together with laminins, proteoglycans and entactin/nidogen.
CC       {ECO:0000256|ARBA:ARBA00003696}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE61522.1}.
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DR   EMBL; AZIM01003856; ETE61522.1; -; Genomic_DNA.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 13.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:ETE61522.1};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT   DOMAIN          1253..1416
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51403"
FT   REGION          73..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..124
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..170
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..575
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..620
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..915
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE61522.1"
SQ   SEQUENCE   1416 AA;  139584 MW;  51A5841DD6174364 CRC64;
     MGAFLIFRGL LAVEKVKKVS KENQAKEGSQ EKMGKLDCQV CLVFPVNLAR LASQEEMETK
     VKKEKLVYLA HLDKPGTGTT VGPKGSKGLA GYPGNKGDRG YPGPVGPPGL PGTPGLPSVG
     PSGPPGLPGE RGQKGDQGLS GIAIPGQPGI DGQPGPRGPP GPPGPPGSTI PPGKVIFLII
     AHQLLVIHLC DKGDTCFNCI GSGIPGPPGE KGFPGLPGDP GLPGPKGDKG VSGVFGAIGP
     QGPPGLPGSP GRPGTKGDPG DMIGFPRMKG EKGNPGFPGP PGLPGLDGSP GKDGLPGRPG
     LKGEPGSIAF KGDRGLTGDP GLPGVVGERG PPGPPGFGPQ GPPGEKGLQG VPGRPGSPGA
     PGPKGEPAQS VPEKGPPGLP GPPGRNGENG FPGEPGQPGS SGLPGIPGQK GEPGFPGIGL
     PGPPGPKGLP GLSGESGLPG NPGRPGADGA PGLPGEKGQK AVKYNSRKHR MDCRVENNYS
     ELTFCFLAFQ GERGHGIPGP KGPAGPPGFK GAQGAKGVSG FPGNPGSPGR AGFDGVPGAK
     GDPGPRGQPG LVGPPGIPGT GVQGPPGPPG SPGPAGSPGF QGIPGEKGDP GQPGFDVPGP
     PGDRGNPGFP GPPGLPGGPG SPGSPGRDGT PGIPGKYILC YSGSVGSKGD MGVMGAPGPL
     GTPGSPGRNG FPGSKGNDGL SGQPGQPGLA GQKGSKGEPG LPGAPGKIDI DHLGSKGQKG
     EPGEKGNPGL TGQKGYPGLP GDPGPAGSVG QPGAPGLPAW KSIQHQSSNN NSVLIGPKGD
     TGIPGGPGPT GPPGLKGANG EMGLPGTPGT KGSQGVPGRV GQPGSPGSPG LKGDKGDPGI
     SGIGIPGPPG PKVGCPHSFQ SCDGNRLLRN QKDCFDGRKR GVSTWTPGIP GLKGLDGPPG
     SPGVPGPPGP PGELGRPGSP GLLGEKGQPG RDGIPGPSGQ KGEPGQPGFG LPGPQGLPGL
     AGKDFILFIS EKESQKGDSG FSGPPGPPGS PGLKGEMGAK GFXFLDHHQK DLRVALGHQA
     YQDGQVRKRS NIKVASIAKR MSTKDICSSS HLFALCKISG VHLGFQVGLP GPEGPRGPPG
     IGGVKGEKGN PGQTGQPGLP GLKGDQGAPG QLGEPGHPGL NGMKGDSGVP GAPGFPGMKG
     PTGPLGPSGP GGDPGPPGSP VVIKGDQGPP GPPGQSGMKG LPGLPGPPGL PGSIGLPGDI
     GRDGLPGFDG PAGRKGERGL SGQPGLRGSQ GPPGPDGLQG PPGVPGTGSV AHGFLITRHS
     QTTDAPFCPP GTNQIYDGFS LLYVQGNERA HGQDLGTAGS CLRRFSTMPF MFCNINNVCN
     FASRNDYSYW LSTPEPMPMS MEPLTGKNIQ PFISRCTVCE APAMVIAVHS QTIQIPSCPQ
     GWNSLWIGYS FMMSETLKAG DLRARISRCQ VCMKRT
//
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